CN115340607A - 抗cd166抗体、可活化抗cd166抗体及其使用方法 - Google Patents
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Families Citing this family (59)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US11089959B2 (en) | 2013-03-15 | 2021-08-17 | I2Dx, Inc. | Electronic delivery of information in personalized medicine |
US9782075B2 (en) | 2013-03-15 | 2017-10-10 | I2Dx, Inc. | Electronic delivery of information in personalized medicine |
CN118146306A (zh) | 2013-09-25 | 2024-06-07 | 西托姆克斯治疗公司 | 基质金属蛋白酶底物和其它可切割部分及其使用方法 |
IL302642A (en) | 2014-01-31 | 2023-07-01 | Cytomx Therapeutics Inc | Polypeptide substrates that activate matriptase and U-plasminogen and other cleavable groups, preparations containing them and their uses |
MA41374A (fr) * | 2015-01-20 | 2017-11-28 | Cytomx Therapeutics Inc | Substrats clivables par métalloprotéase matricielle et clivables par sérine protéase et procédés d'utilisation de ceux-ci |
IL292798A (en) | 2015-05-04 | 2022-07-01 | Cytomx Therapeutics Inc | Anti-cd166 antibodies, activatable anti-cd166 antibodies, preparations containing them and their uses |
EP3484518B1 (en) | 2016-07-07 | 2024-08-14 | The Board of Trustees of the Leland Stanford Junior University | Antibody adjuvant conjugates |
JPWO2018097308A1 (ja) | 2016-11-28 | 2019-10-17 | 中外製薬株式会社 | リガンド結合活性が調整可能なリガンド結合分子 |
EP3546574A4 (en) | 2016-11-28 | 2020-09-09 | Chugai Seiyaku Kabushiki Kaisha | ANTIGEN AND POLYPEPTIDE BINDING AREA INCLUDING A TRANSPORT SECTION |
MX2019006624A (es) | 2016-12-09 | 2019-08-01 | Seattle Genetics Inc | Anticuerpos bivalentes enmascarados por helices superenrolladas. |
CN111133006A (zh) | 2017-07-14 | 2020-05-08 | 西托姆克斯治疗公司 | 抗cd166抗体及其用途 |
EP3668545A2 (en) | 2017-08-16 | 2020-06-24 | Bristol-Myers Squibb Company | Prodruggable antibodies, prodrugs thereof, and methods of use and making |
CN111511762A (zh) | 2017-08-21 | 2020-08-07 | 天演药业公司 | 抗cd137分子及其用途 |
CA3074112A1 (en) * | 2017-08-30 | 2019-03-07 | Cytomx Therapeutics, Inc. | Activatable anti-cd166 antibodies and methods of use thereof |
EP3679068A2 (en) * | 2017-09-08 | 2020-07-15 | Maverick Therapeutics, Inc. | CONDITIONALLY ACTIVATED BINDING MOIETIES CONTAINING Fc REGIONS |
IL302613A (en) | 2017-09-08 | 2023-07-01 | Maverick Therapeutics Inc | Binding proteins are activated under limited conditions |
US20210206845A1 (en) | 2017-11-28 | 2021-07-08 | Chugai Seiyaku Kabushiki Kaisha | Ligand-binding molecule having adjustable ligand-binding activity |
MX2020005220A (es) | 2017-11-28 | 2020-08-24 | Chugai Pharmaceutical Co Ltd | Polipeptido que incluye dominio de union al antigeno y seccion de transporte. |
WO2019148445A1 (en) * | 2018-02-02 | 2019-08-08 | Adagene Inc. | Precision/context-dependent activatable antibodies, and methods of making and using the same |
WO2019148444A1 (en) | 2018-02-02 | 2019-08-08 | Adagene Inc. | Anti-ctla4 antibodies and methods of making and using the same |
US20210020264A1 (en) | 2018-03-20 | 2021-01-21 | Cytomx Therapeutics, Inc. | Systems and methods for quantitative pharmacological modeling of activatable antibody species in mammalian subjects |
CN113840832A (zh) | 2018-05-14 | 2021-12-24 | 狼人治疗公司 | 可活化白介素-2多肽及其使用方法 |
WO2019222294A1 (en) | 2018-05-14 | 2019-11-21 | Werewolf Therapeutics, Inc. | Activatable cytokine polypeptides and methods of use thereof |
JPWO2019230868A1 (ja) | 2018-05-30 | 2021-06-24 | 中外製薬株式会社 | 単ドメイン抗体含有リガンド結合分子 |
TW202029980A (zh) | 2018-10-26 | 2020-08-16 | 美商免疫遺傳股份有限公司 | E p C A M 抗體、可活化抗體及免疫偶聯物以及其用途 |
JP2022512920A (ja) * | 2018-11-02 | 2022-02-07 | シートムエックス セラピューティクス,インコーポレイテッド | 活性化可能抗cd166抗体およびその使用方法 |
US12049505B2 (en) | 2018-12-06 | 2024-07-30 | Cytomx Therapeutics, Inc. | Matrix metalloprotease-cleavable and serine or cysteine protease-cleavable substrates and methods of use thereof |
JP2022517989A (ja) * | 2019-01-14 | 2022-03-11 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | 細胞内部移行をモジュレートするための組成物および方法 |
CN113677372A (zh) * | 2019-02-26 | 2021-11-19 | 西托姆克斯治疗公司 | 可活化免疫检查点抑制剂和经缀合可活化抗体的组合疗法 |
CN114390938A (zh) | 2019-03-05 | 2022-04-22 | 武田药品工业有限公司 | 受约束的条件性活化的结合蛋白 |
CN113993549A (zh) | 2019-03-15 | 2022-01-28 | 博尔特生物治疗药物有限公司 | 靶向her2的免疫缀合物 |
US11833214B2 (en) | 2019-03-21 | 2023-12-05 | Immunogen, Inc. | Methods of preparing cell-binding agent-drug conjugates |
KR102212149B1 (ko) * | 2019-03-28 | 2021-02-04 | 부산대학교 산학협력단 | 암 줄기세포에 특이적으로 결합하는 압타머 및 이의 용도 |
LT3958977T (lt) | 2019-04-26 | 2023-12-27 | Immunogen, Inc. | Kamptotecino dariniai |
SG11202112541RA (en) | 2019-05-14 | 2021-12-30 | Werewolf Therapeutics Inc | Separation moieties and methods and use thereof |
US20220226514A1 (en) * | 2019-05-17 | 2022-07-21 | Cytomx Therapeutics, Inc. | Methods and compositions for determining the biodistribution of activatable anti-cd166 antibody conjugates |
MX2021014433A (es) | 2019-06-05 | 2022-03-11 | Chugai Pharmaceutical Co Ltd | Molecula de union a sitio de escision de anticuerpo. |
US20220251206A1 (en) | 2019-06-11 | 2022-08-11 | Bristol-Myers Squibb Company | Anti-ctla4 antibody prodruggable (probody) at a cdr position |
WO2021061867A1 (en) * | 2019-09-23 | 2021-04-01 | Cytomx Therapeutics, Inc. | Anti-cd47 antibodies, activatable anti-cd47 antibodies, and methods of use thereof |
KR20220101147A (ko) | 2019-11-14 | 2022-07-19 | 웨어울프 세라퓨틱스, 인크. | 활성화가능한 사이토카인 폴리펩티드 및 이의 사용 방법 |
AU2021254279A1 (en) | 2020-04-09 | 2022-11-10 | Cytomx Therapeutics, Inc. | Compositions containing activatable antibodies |
EP4243851A1 (en) * | 2020-11-16 | 2023-09-20 | The Cleveland Clinic Foundation | Anti-cd6 antibody conjugates for treating t-cell and b-cell mediated disorders, and t-cell and b-cell cancers |
AU2022218137A1 (en) | 2021-02-03 | 2023-08-24 | Mozart Therapeutics, Inc. | Binding agents and methods of using the same |
AU2022367525A1 (en) | 2021-10-15 | 2024-05-02 | Amgen Inc. | Activatable polypeptide complex |
WO2023076876A1 (en) | 2021-10-26 | 2023-05-04 | Mozart Therapeutics, Inc. | Modulation of immune responses to viral vectors |
WO2023086897A1 (en) * | 2021-11-12 | 2023-05-19 | University Of Florida Research Foundation, Incorporated | Siglec-6 antibodies, derivative compounds and related uses |
CN114621348B (zh) * | 2022-01-24 | 2023-09-22 | 深圳市乐土生物医药有限公司 | 一种多肽及其抗磷脂酰肌醇蛋白聚糖3抗体 |
WO2023183888A1 (en) | 2022-03-23 | 2023-09-28 | Cytomx Therapeutics, Inc. | Activatable antigen-binding protein constructs and uses of the same |
WO2023183923A1 (en) | 2022-03-25 | 2023-09-28 | Cytomx Therapeutics, Inc. | Activatable dual-anchored masked molecules and methods of use thereof |
WO2023192606A2 (en) | 2022-04-01 | 2023-10-05 | Cytomx Therapeutics, Inc. | Cd3-binding proteins and methods of use thereof |
WO2023192973A1 (en) | 2022-04-01 | 2023-10-05 | Cytomx Therapeutics, Inc. | Activatable multispecific molecules and methods of use thereof |
WO2023222580A1 (en) | 2022-05-16 | 2023-11-23 | Byondis B.V. | Novel masked antibodies |
WO2024015830A1 (en) | 2022-07-12 | 2024-01-18 | Cytomx Therapeutics, Inc. | Epcam immunoconjugates and uses thereof |
TW202426637A (zh) | 2022-08-01 | 2024-07-01 | 美商Cytomx生物製藥公司 | 蛋白酶可切割受質及其使用方法 |
WO2024030850A1 (en) | 2022-08-01 | 2024-02-08 | Cytomx Therapeutics, Inc. | Protease-cleavable substrates and methods of use thereof |
WO2024030847A1 (en) | 2022-08-01 | 2024-02-08 | Cytomx Therapeutics, Inc. | Protease-cleavable moieties and methods of use thereof |
WO2024030843A1 (en) | 2022-08-01 | 2024-02-08 | Cytomx Therapeutics, Inc. | Protease-cleavable moieties and methods of use thereof |
WO2024030845A1 (en) | 2022-08-01 | 2024-02-08 | Cytomx Therapeutics, Inc. | Protease-cleavable moieties and methods of use thereof |
WO2024040194A1 (en) | 2022-08-17 | 2024-02-22 | Capstan Therapeutics, Inc. | Conditioning for in vivo immune cell engineering |
Family Cites Families (56)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3773919A (en) | 1969-10-23 | 1973-11-20 | Du Pont | Polylactide-drug mixtures |
US4485045A (en) | 1981-07-06 | 1984-11-27 | Research Corporation | Synthetic phosphatidyl cholines useful in forming liposomes |
US4522811A (en) | 1982-07-08 | 1985-06-11 | Syntex (U.S.A.) Inc. | Serial injection of muramyldipeptides and liposomes enhances the anti-infective activity of muramyldipeptides |
US4544545A (en) | 1983-06-20 | 1985-10-01 | Trustees University Of Massachusetts | Liposomes containing modified cholesterol for organ targeting |
WO1988001513A1 (en) | 1986-08-28 | 1988-03-10 | Teijin Limited | Cytocidal antibody complex and process for its preparation |
US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
US5013556A (en) | 1989-10-20 | 1991-05-07 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
US5151510A (en) | 1990-04-20 | 1992-09-29 | Applied Biosystems, Inc. | Method of synethesizing sulfurized oligonucleotide analogs |
DE69329503T2 (de) | 1992-11-13 | 2001-05-03 | Idec Pharma Corp | Therapeutische Verwendung von chimerischen und markierten Antikörpern, die gegen ein Differenzierung-Antigen gerichtet sind, dessen Expression auf menschliche B Lymphozyt beschränkt ist, für die Behandlung von B-Zell-Lymphoma |
US5998172A (en) | 1993-11-02 | 1999-12-07 | Duke University | Anti-CD6 ligand antibodies |
WO1999011287A1 (en) | 1997-09-04 | 1999-03-11 | Osiris Therapeutics, Inc. | Ligands that modulate differentiation of mesenchymal stem cells |
US6302855B1 (en) | 1998-05-20 | 2001-10-16 | Novo Nordisk A/S | Medical apparatus for use by a patient for medical self treatment of diabetes |
EP1286700A2 (en) | 2000-06-01 | 2003-03-05 | Universite Catholique De Louvain | Tumor activated prodrug compounds |
US7465790B2 (en) | 2000-10-09 | 2008-12-16 | Isis Innovation, Inc. | Therapeutic antibodies |
CA2423850C (en) | 2000-10-09 | 2017-07-04 | Isis Innovation Limited | Therapeutic antibodies |
AU2003225294A1 (en) | 2002-05-03 | 2003-11-17 | Raven Biotechnologies, Inc. | Alcam and alcam modulators |
US20040109855A1 (en) | 2002-07-23 | 2004-06-10 | Herman Waldmann | Therapeutic antibodies with reduced side effect |
AU2003265866A1 (en) | 2002-09-03 | 2004-03-29 | Vit Lauermann | Targeted release |
RU2362780C2 (ru) | 2003-12-22 | 2009-07-27 | Глаксо Груп Лимитед | Nogo-a-нейтрализующие иммуноглобулины для лечения неврологических заболеваний |
EP1930346B1 (en) | 2005-08-29 | 2011-10-19 | Japan Science and Technology Agency | Antibody produced using ostrich and method for production thereof |
AU2006284651C1 (en) | 2005-08-31 | 2013-09-12 | The Regents Of The University Of California | Cellular libraries of peptide sequences (CLiPS) and methods of using the same |
US7582441B1 (en) | 2005-10-17 | 2009-09-01 | Celera Corporation | Methods and compositions for treating and diagnosing disease |
JP5612247B2 (ja) | 2005-11-29 | 2014-10-22 | 独立行政法人科学技術振興機構 | Cd166に対するモノクローナル抗体およびその産生方法 |
EP1993608A1 (en) | 2006-03-10 | 2008-11-26 | Diatos | Anticancer drugs conjugated to antibody via an enzyme cleavable linker |
EP2975057A1 (en) | 2006-07-10 | 2016-01-20 | Fujita Health University | Novel anti-cd73 antibody |
GB0705775D0 (en) | 2007-03-26 | 2007-05-02 | Affitech As | Product |
JP2009055899A (ja) | 2007-08-07 | 2009-03-19 | Igaku Seibutsugaku Kenkyusho:Kk | Adcc活性を増強させた抗体及びその製造方法 |
CA2697032C (en) | 2007-08-22 | 2021-09-14 | The Regents Of The University Of California | Activatable binding polypeptides and methods of identification and use thereof |
CA2699394C (en) | 2007-09-17 | 2020-03-24 | The Regents Of The University Of California | Internalizing human monoclonal antibodies targeting prostate cancer cells in situ |
KR20100117120A (ko) | 2008-02-20 | 2010-11-02 | 지투 인플레메이션 피티와이 엘티디 | 인간화된 항-C5aR 항체 |
EP2276506A4 (en) | 2008-04-30 | 2014-05-07 | Immunogen Inc | EFFICIENT CONJUGATES AND HYDROPHILIC BINDER |
EP2388320B1 (en) | 2008-12-22 | 2017-02-15 | Chugai Seiyaku Kabushiki Kaisha | Anti-hs6st2 antibodies and uses thereof |
CN102482347B (zh) | 2009-01-12 | 2017-04-26 | 希托马克斯医疗有限责任公司 | 修饰抗体组合物及其制备和使用方法 |
ES2641612T3 (es) | 2009-04-17 | 2017-11-10 | Immunas Pharma, Inc. | Anticuerpos que se unen específicamente a oligómeros de beta A y uso de los mismos |
WO2010129609A2 (en) | 2009-05-07 | 2010-11-11 | The Regents Of The University Of California | Antibodies and methods of use thereof |
MX2013005046A (es) | 2010-11-03 | 2013-12-12 | Immunogen Inc | Agentes citotoxicos que comprenden nuevos derivados de ansamitocina. |
AU2012253373A1 (en) * | 2011-05-11 | 2013-11-28 | Nanovalent Pharmaceuticals, Inc. | Enhanced growth inhibition of osteosarcoma by cytotoxic polymerized liposomal nanoparticles targeting the alcam cell surface receptor |
RU2713121C2 (ru) * | 2012-04-27 | 2020-02-03 | Сайтомкс Терапьютикс, Инк. | Активируемые антитела, которые связываются с рецептором эпидермального фактора роста, и способы их применения |
WO2013192546A1 (en) | 2012-06-22 | 2013-12-27 | Cytomx Therapeutics, Inc. | Activatable antibodies having non-binding steric moieties and mehtods of using the same |
US9309510B2 (en) | 2012-08-10 | 2016-04-12 | Cytomx Therapeutics, Inc. | Protease-resistant systems for polypeptide display and methods of making and using thereof |
JP2016509582A (ja) | 2012-12-19 | 2016-03-31 | アンプリミューン, インコーポレイテッド | 抗ヒトb7−h4抗体およびその使用 |
WO2014107599A2 (en) | 2013-01-04 | 2014-07-10 | Cytomx Therapeutics, Inc. | Compositions and methods for detecting protease activity in biological systems |
WO2014134483A2 (en) | 2013-02-28 | 2014-09-04 | Immunogen, Inc. | Conjugates comprising cell-binding agents and cytotoxic agents |
US9517276B2 (en) * | 2013-06-04 | 2016-12-13 | Cytomx Therapeutics, Inc. | Compositions and methods for conjugating activatable antibodies |
IL292798A (en) | 2015-05-04 | 2022-07-01 | Cytomx Therapeutics Inc | Anti-cd166 antibodies, activatable anti-cd166 antibodies, preparations containing them and their uses |
EP3325006A4 (en) | 2015-07-17 | 2019-03-06 | The Trustees of Columbia University in the City of New York | METHOD FOR TREATING CD166-EXPRESSIVE CANCER |
EP3371301A4 (en) | 2015-11-04 | 2019-06-26 | Fate Therapeutics, Inc. | METHOD AND COMPOSITIONS FOR INDUCING THE DIFFERENTIATION OF HEMATOPOIETIC CELLS |
WO2017218750A1 (en) | 2016-06-15 | 2017-12-21 | The Cleveland Clinic Foundation | Novel anti-cd6 antibodies for treating t-cell mediated conditions |
JP6183523B2 (ja) | 2016-09-14 | 2017-08-23 | 株式会社アンセイ | 車両用開閉体の開閉装置及び車両用開閉体の開閉装置用リンク機構 |
WO2018067991A1 (en) | 2016-10-07 | 2018-04-12 | The Brigham And Women's Hospital, Inc. | Modulation of novel immune checkpoint targets |
WO2018071058A1 (en) | 2016-10-15 | 2018-04-19 | Baylor College Of Medicine | Platform for enhanced targeted cell delivery |
NZ759442A (en) | 2017-06-01 | 2024-07-05 | Cytomx Therapeutics Inc | Activatable anti-pdl1 antibodies, and methods of use thereof |
CN111133006A (zh) | 2017-07-14 | 2020-05-08 | 西托姆克斯治疗公司 | 抗cd166抗体及其用途 |
CA3074112A1 (en) | 2017-08-30 | 2019-03-07 | Cytomx Therapeutics, Inc. | Activatable anti-cd166 antibodies and methods of use thereof |
JP2022512920A (ja) | 2018-11-02 | 2022-02-07 | シートムエックス セラピューティクス,インコーポレイテッド | 活性化可能抗cd166抗体およびその使用方法 |
CN113677372A (zh) | 2019-02-26 | 2021-11-19 | 西托姆克斯治疗公司 | 可活化免疫检查点抑制剂和经缀合可活化抗体的组合疗法 |
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